HIV molecular immunology database
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|MAb ID||588-D (588)|
|HXB2 Location||Env||Env Epitope Map|
|Research Contact||Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu), NYU Med Center, NY, NY|
|Ab Type||gp120 CD4BS|
|Keywords||antibody binding site, antibody generation|
Showing 7 of 7 notes.
Showing 7 of 7 references.
Karwowska1992 S. Karwowska, M. K. Gorny, A. Buchbinder, V. Gianakakos, C. Williams, T. Fuerst, and S. Zolla-Pazner. Production of human monoclonal antibodies specific for conformational and linear non-V3 epitopes of gp120. AIDS Res. Hum. Retroviruses, 8:1099-1106, 1992. A single linear MAb was generated, to the immunodominant domain in the C-terminal portion of gp120. This antibody did not inhibit rCD4-rgp120 binding or neutralize IIIB or MN. Three conformational epitope binding MAbs were also described in this paper that could neutralize IIIB and MN. PubMed ID: 1380257. Show all entries for this paper.
Buchbinder1992 A. Buchbinder, S. Karwowska, M. K. Gorny, S. T. Burda, and S. Zolla-Pazner. Synergy between Human Monoclonal Antibodies to HIV Extends Their Effective Biologic Activity against Homologous and Divergent Strains. AIDS Res. Hum. Retroviruses, 8:425-427, 1992. The anti-gp120 V3 MAb 447-D and the anti- gp120 CD4 BS MAb 588-D showed synergistic neutralization. PubMed ID: 1466965. Show all entries for this paper.
Moore1993a J. P. Moore and D. D. Ho. Antibodies to discontinuous or conformationally sensitive epitopes on the gp120 glycoprotein of human immunodeficiency virus type 1 are highly prevalent in sera of infected humans. J. Virol., 67:863-875, 1993. CD4BS antibodies are prevalent in HIV-1-positive sera, while neutralizing MAbs to C4, V2, and V3 and MAbs to linear epitopes are less common. Most linear epitope MAbs in human sera are directed against the V3 region, and cross-reactive MAbs tend to be directed against discontinuous epitopes. PubMed ID: 7678308. Show all entries for this paper.
Jeffs1996 S. A. Jeffs, J. McKeating, S. Lewis, H. Craft, D. Biram, P. E. Stephens, and R. L. Brady. Antigenicity of truncated forms of the human immunodeficiency virus type 1 envelope glycoprotein. J. Gen. Virol., 77:1403-1410, 1996. PubMed ID: 8757980. Show all entries for this paper.
Nyambi1998 P. N. Nyambi, M. K. Gorny, L. Bastiani, G. van der Groen, C. Williams, and S. Zolla-Pazner. Mapping of Epitopes Exposed on Intact Human Immunodeficiency Virus Type 1 (HIV-1) Virions: A New Strategy for Studying the Immunologic Relatedness of HIV-1. J. Virol., 72:9384-9391, 1998. 18 human MAbs binding to gp120 and gp41 were tested using a novel assay to test binding to intact HIV-1 virions. The new method involves using MAbs to the host proteins incorporated into virions to bind them to ELIZA plates. Antigenic conservation in epitopes of HIV-1 in clades A, B, D, F, G, and H was studied. MAbs were selected that were directed against V2, V3, CD4bd, C5 or gp41 regions. Antibodies against V2, the CD4BS, and sp41 showed weak and sporadic reactivities, while binding strongly to gp120, suggesting these epitopes are hidden when gp120 is in its native, quaternary structure. PubMed ID: 9765494. Show all entries for this paper.
Hioe2000 C. E. Hioe, G. J. Jones, A. D. Rees, S. Ratto-Kim, D. Birx, C. Munz, M. K. Gorny, M. Tuen, and S. Zolla-Pazner. Anti-CD4-Binding Domain Antibodies Complexed with HIV Type 1 Glycoprotein 120 Inhibit CD4+ T Cell-Proliferative Responses to Glycoprotein 120. AIDS Res. Hum. Retroviruses, 16:893-905, 2000. PubMed ID: 10875615. Show all entries for this paper.
Nyambi2000 P. N. Nyambi, H. A. Mbah, S. Burda, C. Williams, M. K. Gorny, A. Nadas, and S. Zolla-Pazner. Conserved and Exposed Epitopes on Intact, Native, Primary Human Immunodeficiency Virus Type 1 Virions of Group M. J. Virol., 74:7096-7107, 2000. PubMed ID: 10888650. Show all entries for this paper.